Maturation-related change of the protein kinase activity in the rabbit red blood cells.
The protein kinase activity of rabbit reticulocyte and erythrocyte hemolysate is due to multiple forms (casein kinases and histone kinases) which have been partially purified by Sepharose 6B filtration followed by phosphocellulose chromatography in the presence of 0.2% Triton X-100. The casein kinase activity is resolved by such a procedure into two forms differing in catalytic properties: i.e. the casein kinase TS phosphorylates both serine and threonine residues of casein, while the casein kinase S phosphorylates only serine residues. The comparative results indicate that during differentiation and maturation of rabbit red blood cells multiple cytosol protein kinase activities markedly decrease, while the casein kinase S does not change significantly.
D000818:Animals; D047388:Casein Kinases; D002454:Cell Differentiation; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D004905:Erythrocyte Aging; D004912:Erythrocytes / Q000201:enzymology*; D017830:Octoxynol; D011092:Polyethylene Glycols; D011494:Protein Kinases / Q000097:blood* / Q000302:isolation & purification; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology; D012694:Serine / Q000378:metabolism; D013912:Threonine / Q000378:metabolism
D013912:Threonine; D011092:Polyethylene Glycols; D012694:Serine; D017830:Octoxynol; D011494:Protein Kinases; D047388:Casein Kinases